Loading
PDBj
MenuPDBj@FacebookPDBj@TwitterPDBj@YouTubewwPDB FoundationwwPDB
RCSB PDBPDBeBMRBAdv. SearchSearch help

3QG5

The Mre11:Rad50 complex forms an ATP dependent molecular clamp in DNA double-strand break repair

Functional Information from GO Data
ChainGOidnamespacecontents
A0006302biological_processdouble-strand break repair
A0016887molecular_functionATP hydrolysis activity
B0006302biological_processdouble-strand break repair
B0016887molecular_functionATP hydrolysis activity
C0003677molecular_functionDNA binding
C0004519molecular_functionendonuclease activity
C0004520molecular_functionDNA endonuclease activity
C0004527molecular_functionexonuclease activity
C0004529molecular_functionDNA exonuclease activity
C0005515molecular_functionprotein binding
C0006259biological_processDNA metabolic process
C0006260biological_processDNA replication
C0006281biological_processDNA repair
C0006302biological_processdouble-strand break repair
C0006310biological_processDNA recombination
C0008408molecular_function3'-5' exonuclease activity
C0016787molecular_functionhydrolase activity
C0046872molecular_functionmetal ion binding
D0003677molecular_functionDNA binding
D0004519molecular_functionendonuclease activity
D0004520molecular_functionDNA endonuclease activity
D0004527molecular_functionexonuclease activity
D0004529molecular_functionDNA exonuclease activity
D0005515molecular_functionprotein binding
D0006259biological_processDNA metabolic process
D0006260biological_processDNA replication
D0006281biological_processDNA repair
D0006302biological_processdouble-strand break repair
D0006310biological_processDNA recombination
D0008408molecular_function3'-5' exonuclease activity
D0016787molecular_functionhydrolase activity
D0046872molecular_functionmetal ion binding
Functional Information from PDB Data
site_idAC1
Number of Residues4
DetailsBINDING SITE FOR RESIDUE GOL D 3968
ChainResidue
CLEU75
CPHE102
DLYS97
DPHE102

site_idAC2
Number of Residues2
DetailsBINDING SITE FOR RESIDUE GOL A 3968
ChainResidue
AARG136
AGLU144

Functional Information from PROSITE/UniProt
site_idPS00211
Number of Residues15
DetailsABC_TRANSPORTER_1 ABC transporters family signature. LSGGERALISISLAM
ChainResidueDetails
ALEU767-MSE781

Functional Information from SwissProt/UniProt
site_idSWS_FT_FI1
Number of Residues2
DetailsACT_SITE: Proton donor => ECO:0000250|UniProtKB:Q8U1N9, ECO:0000255|HAMAP-Rule:MF_02044
ChainResidueDetails
CHIS94
DHIS94

site_idSWS_FT_FI2
Number of Residues8
DetailsBINDING: BINDING => ECO:0000269|PubMed:21937514, ECO:0000269|PubMed:24316220, ECO:0007744|PDB:3THN, ECO:0007744|PDB:3THO, ECO:0007744|PDB:4NZV, ECO:0007744|PDB:4O24, ECO:0007744|PDB:4O43, ECO:0007744|PDB:4O4K, ECO:0007744|PDB:4O5G
ChainResidueDetails
CASP14
CHIS16
CASP58
CHIS216
DASP14
DHIS16
DASP58
DHIS216

site_idSWS_FT_FI3
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21937514, ECO:0000269|PubMed:24316220, ECO:0007744|PDB:3THN, ECO:0007744|PDB:3THO, ECO:0007744|PDB:4NZV, ECO:0007744|PDB:4O24, ECO:0007744|PDB:4O4K
ChainResidueDetails
CHIS180
BARG63
DHIS180
ASER38
AARG53
AARG63
BGLY35
BLYS36
BSER38
BARG53

site_idSWS_FT_FI4
Number of Residues2
DetailsBINDING: BINDING => ECO:0000269|PubMed:21937514, ECO:0000269|PubMed:24316220, ECO:0007744|PDB:4NZV
ChainResidueDetails
CHIS218
DHIS218
BSER37
BGLN142

site_idSWS_FT_FI5
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:21458667, ECO:0000305|PubMed:25349191, ECO:0007744|PDB:3QF7, ECO:0007744|PDB:3THO, ECO:0007744|PDB:4W9M
ChainResidueDetails
AASP59
BASP59

site_idSWS_FT_FI6
Number of Residues2
DetailsBINDING: BINDING => ECO:0000305|PubMed:21458667, ECO:0000305|PubMed:21937514, ECO:0007744|PDB:3QF7, ECO:0007744|PDB:3THO
ChainResidueDetails
AVAL61
BVAL61

site_idSWS_FT_FI7
Number of Residues2
DetailsBINDING: BINDING => ECO:0007744|PDB:4W9M
ChainResidueDetails
AASP797
BASP797

222415

PDB entries from 2024-07-10

PDB statisticsPDBj update infoContact PDBjnumon